Preventing protein haze in bottled white wine

  • Waters E
  • Alexander G
  • Muhlack R
 et al. 
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Abstract

Slow denaturation of wine proteins is thought to lead to protein aggregation, flocculation into a hazy suspension and formation of precipitates. The majority of wine proteins responsible for haze are grape-derived, have low isoelectric points and molecular weight. They are grape pathogenesis-related (PR) proteins that are expressed throughout the ripening period post véraison, and are highly resistant to low pH and enzymatic or non-enzymatic proteolysis. Protein levels in un-fined white wine differ by variety and range up to 300 mg/L. Infection with some common grapevine pathogens or skin contact, such as occurs during transport of mechanically harvested fruit, results in enhanced concentrations of some PR proteins in juice and wine. Oenological control of protein instability is achieved through adsorption of wine proteins onto bentonite. The adsorption of proteins onto bentonite occurs within several minutes, suggesting that a continuous contacting process could be developed. The addition of proteolytic enzyme during short term heat exposure, to induce PR protein denaturation, showed promise as an alternative to bentonite fining. The addition of haze-protective factors, yeast mannoproteins, to wines results in decreased particle size of haze, probably by competition with wine proteins for other non-proteinaceous wine components required for the formation of large insoluble aggregations of protein. Other wine components likely to influence haze formation are ethanol concentration, pH, metal ions and phenolic compounds.

Author-supplied keywords

  • Bentonite
  • Botrytis
  • Chitinase
  • Grape
  • Haze
  • Heat
  • Heat test
  • Maturity
  • Mechanical harvesting
  • Pathogenesis-related
  • Powdery mildew
  • Protein
  • Protein instability
  • Proteolytic enzymes
  • Ripening
  • Sediment
  • Thaumatin-like
  • Turbidity
  • Uncinula
  • Vitis vinifera
  • White wine

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Authors

  • E. J. Waters

  • G. Alexander

  • R. Muhlack

  • K. F. Pocock

  • C. Colby

  • B. K. O'Neill

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